The role of retinal light induced dipole in halorhodopsin structural alteration

Sansa Dutta; Amiram Hirshfeld; Mordechai Sheves

doi:10.1016/j.febslet.2015.10.005

The role of retinal light induced dipole in halorhodopsin structural alteration

Sansa Dutta, Amiram Hirshfeld, Mordechai Sheves

Department of Molecular Chemistry and Materials Science

Weizmann Institute of Science

Research output: Contribution to journal › Article › peer-review

Abstract

The present work studies the mechanism of light induced protein conformational changes in the over-expressed mutant of halorhodopsin (phR) from Natronomonas pharaonis. The catalytic effect of light is reflected in accelerating hydroxyl amine reaction rate of light adapted phR. Light catalysis was detected in native phR but also in artificial pigments derived from tailored retinal analogs locked at the crucial C₁₃=C₁₄ double bond. It is proposed that the photoexcited retinal chromophore induces protein concerted motion that decreases the energy gap between reactants ground and transition states. This energy gap is overcome by coupling to specific protein vibrations. Surprisingly, the rate constants show unusual decreasing trend following temperature increase both for native and artificial pigments.

Original language	English
Pages (from-to)	3576-3580
Number of pages	5
Journal	FEBS Letters
Volume	589
Issue number	23
DOIs	https://doi.org/10.1016/j.febslet.2015.10.005
State	Published - 30 Nov 2015

All Science Journal Classification (ASJC) codes

Genetics
Molecular Biology
Biophysics
Structural Biology
Biochemistry
Cell Biology

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10.1016/j.febslet.2015.10.005

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title = "The role of retinal light induced dipole in halorhodopsin structural alteration",

abstract = "The present work studies the mechanism of light induced protein conformational changes in the over-expressed mutant of halorhodopsin (phR) from Natronomonas pharaonis. The catalytic effect of light is reflected in accelerating hydroxyl amine reaction rate of light adapted phR. Light catalysis was detected in native phR but also in artificial pigments derived from tailored retinal analogs locked at the crucial C13=C14 double bond. It is proposed that the photoexcited retinal chromophore induces protein concerted motion that decreases the energy gap between reactants ground and transition states. This energy gap is overcome by coupling to specific protein vibrations. Surprisingly, the rate constants show unusual decreasing trend following temperature increase both for native and artificial pigments.",

author = "Sansa Dutta and Amiram Hirshfeld and Mordechai Sheves",

note = "Publisher Copyright: {\textcopyright} 2015 Federation of European Biochemical Societies.",

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AU - Hirshfeld, Amiram

AU - Sheves, Mordechai

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Y1 - 2015/11/30

N2 - The present work studies the mechanism of light induced protein conformational changes in the over-expressed mutant of halorhodopsin (phR) from Natronomonas pharaonis. The catalytic effect of light is reflected in accelerating hydroxyl amine reaction rate of light adapted phR. Light catalysis was detected in native phR but also in artificial pigments derived from tailored retinal analogs locked at the crucial C13=C14 double bond. It is proposed that the photoexcited retinal chromophore induces protein concerted motion that decreases the energy gap between reactants ground and transition states. This energy gap is overcome by coupling to specific protein vibrations. Surprisingly, the rate constants show unusual decreasing trend following temperature increase both for native and artificial pigments.

AB - The present work studies the mechanism of light induced protein conformational changes in the over-expressed mutant of halorhodopsin (phR) from Natronomonas pharaonis. The catalytic effect of light is reflected in accelerating hydroxyl amine reaction rate of light adapted phR. Light catalysis was detected in native phR but also in artificial pigments derived from tailored retinal analogs locked at the crucial C13=C14 double bond. It is proposed that the photoexcited retinal chromophore induces protein concerted motion that decreases the energy gap between reactants ground and transition states. This energy gap is overcome by coupling to specific protein vibrations. Surprisingly, the rate constants show unusual decreasing trend following temperature increase both for native and artificial pigments.

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DO - 10.1016/j.febslet.2015.10.005

M3 - مقالة

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EP - 3580

JO - FEBS Letters

JF - FEBS Letters

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ER -

The role of retinal light induced dipole in halorhodopsin structural alteration

Abstract

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